Zipper hypothesis

Mack, J. W., Steven, A. C., and Steinert, P. M. (1993). The mechanism of interaction of filaggrin with intermediate filaments. The ionic zipper hypothesis./. Mol. Biol. 232, 50-66. 

The crystal structure of both ribonuclease A and S have been determined and residues 2-13 form two-three turns of a-helix (4,). In the dissociated state, S-peptide contains little detectable helix either by circular dichroism (5) or by NMR (6,7). Either the S-protein induces the bound conformation during the association or a conformer too limited in concentration to be detected by spectroscopy is preferentially bound. It has been argued (3) on kinetic grounds that the induced-fit or "zipper" hypothesis is more likely, but no relevant experimental data exists on this or other systems to our knowledge. 

Could the secondary structure frequently observed in heat denatured proteins result in some cases from aggregation and not be a residual one One could imagine a mechanism analogous to the hydrophobic zipper hypothesis of Dill et al. [160] acting at the inter-molecular level. 

The oligomeric state of functional nucleotide sugar transporters has been proposed to be the homodimer. This hypothesis was established on the basis of structural analogy existing between nucleotide sugar transporters and the Golgi transporter for activated sulfate, which is a dimer in its active state [60]. The identification of potential leucine zipper motifs in some of the cloned nucleotide sugar transporters supported this hypothesis [3]. However, the importance of the leucine zipper motifs... 

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